Datasheet

Biological Description

Specificity	Glucose 6 Phosphate Dehydrogenase Rabbit mAb detects endogenous levels of total Glucose 6 Phosphate Dehydrogenase protein.
Background	Glucose-6-phosphate dehydrogenase (G6PD) is the rate-limiting enzyme of the pentose phosphate pathway (PPP) and plays a fundamental role in cellular redox balance. Its primary physiological function is to generate nicotinamide adenine dinucleotide phosphate (NADPH), which provides reducing power to specific cells, particularly erythrocytes, thereby protecting them from oxidative damage. By sustaining the intracellular NADPH pool, G6PD is essential for redox homeostasis in healthy individuals. Functioning as a classical oxidoreductase, G6PD activity is tightly regulated by post-translational modifications. Acetylation at Lys-403 by ELP3 suppresses its activity by preventing homodimerization, whereas deacetylation at the same site by SIRT2 enhances enzymatic function. The enzyme catalyzes the oxidative conversion of D-glucose-6-phosphate to D-ribulose-5-phosphate, a key step in the PPP. Mutations in the G6PD gene at various positions can impair substrate binding, reducing production of D-ribulose-5-phosphate and overall enzyme efficiency. G6PD is also highly susceptible to phosphorylation, which is thought to contribute significantly to loss of activity and the onset of hemolytic anemia. Deficiency in G6PD disrupts redox equilibrium, leading to impaired cell signaling, abnormal cell growth, developmental defects, and altered susceptibility to infections. Although ubiquitously expressed with a housekeeping role across tissues, G6PD is particularly vital for the structural integrity and survival of red blood cells, which rely heavily on NADPH for protection against oxidative stress.

Specificity

Glucose 6 Phosphate Dehydrogenase Rabbit mAb detects endogenous levels of total Glucose 6 Phosphate Dehydrogenase protein.

Background

Glucose-6-phosphate dehydrogenase (G6PD) is the rate-limiting enzyme of the pentose phosphate pathway (PPP) and plays a fundamental role in cellular redox balance. Its primary physiological function is to generate nicotinamide adenine dinucleotide phosphate (NADPH), which provides reducing power to specific cells, particularly erythrocytes, thereby protecting them from oxidative damage. By sustaining the intracellular NADPH pool, G6PD is essential for redox homeostasis in healthy individuals. Functioning as a classical oxidoreductase, G6PD activity is tightly regulated by post-translational modifications. Acetylation at Lys-403 by ELP3 suppresses its activity by preventing homodimerization, whereas deacetylation at the same site by SIRT2 enhances enzymatic function. The enzyme catalyzes the oxidative conversion of D-glucose-6-phosphate to D-ribulose-5-phosphate, a key step in the PPP. Mutations in the G6PD gene at various positions can impair substrate binding, reducing production of D-ribulose-5-phosphate and overall enzyme efficiency. G6PD is also highly susceptible to phosphorylation, which is thought to contribute significantly to loss of activity and the onset of hemolytic anemia. Deficiency in G6PD disrupts redox equilibrium, leading to impaired cell signaling, abnormal cell growth, developmental defects, and altered susceptibility to infections. Although ubiquitously expressed with a housekeeping role across tissues, G6PD is particularly vital for the structural integrity and survival of red blood cells, which rely heavily on NADPH for protection against oxidative stress.

Usage Information

Application

WB, IP, IHC, IF, FCM

Dilution

WB	IP	IHC	IF	FCM
1:1000	1:40	1:2000	1:100	1:400

Reactivity

Mouse, Rat, Human

Source

Rabbit

MW

59 kDa

Storage Buffer

PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage
(from the date of receipt)

-20°C (avoid freeze-thaw cycles), 2 years

Exprimental Methods

References

https://pubmed.ncbi.nlm.nih.gov/30258923/

Glucose 6 Phosphate Dehydrogenase Rabbit mAb

Biological Description

Usage Information

References

Application Data